JPH02104595A - 非ペプチドのペプチド相当物及びそのデザイン方法 - Google Patents

非ペプチドのペプチド相当物及びそのデザイン方法

Info

Publication number: JPH02104595A
Authority: JP; Japan
Prior art keywords: polypeptide; peptide; ouabain; amino acid; nucleotide sequence
Prior art date: 1988-03-04
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Pending

Application number

JP1050208A

Other languages

English (en)

Japanese (ja)

Inventor

Jimmy D Neill

ジミー　デイ　ネイル

Edwin J Blalock

ジエイ　エドウイン　ブラロツク

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

University of Alabama UA

University of Alabama at Birmingham UAB

Original Assignee

University of Alabama UA

University of Alabama at Birmingham UAB

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1988-03-04

Filing date

1989-03-03

Publication date

1990-04-17

1989-03-03 Application filed by University of Alabama UA, University of Alabama at Birmingham UAB filed Critical University of Alabama UA

1990-04-17 Publication of JPH02104595A publication Critical patent/JPH02104595A/ja

Status Pending legal-status Critical Current

Links

108090000765 processed proteins & peptides Proteins 0.000 title claims description 241
102000004196 processed proteins & peptides Human genes 0.000 title claims description 116
238000000034 method Methods 0.000 title claims description 25
238000013461 design Methods 0.000 title description 7
230000000295 complement effect Effects 0.000 claims description 77
230000027455 binding Effects 0.000 claims description 57
229960003343 ouabain Drugs 0.000 claims description 48
229920001184 polypeptide Polymers 0.000 claims description 46
LPMXVESGRSUGHW-UHFFFAOYSA-N Acolongiflorosid K Natural products OC1C(O)C(O)C(C)OC1OC1CC2(O)CCC3C4(O)CCC(C=5COC(=O)C=5)C4(C)CC(O)C3C2(CO)C(O)C1 LPMXVESGRSUGHW-UHFFFAOYSA-N 0.000 claims description 38
LPMXVESGRSUGHW-GHYGWZAOSA-N Ouabain Natural products O([C@@H]1[C@@H](O)[C@@H](O)[C@@H](O)[C@H](C)O1)[C@H]1C[C@@H](O)[C@@]2(CO)[C@@](O)(C1)CC[C@H]1[C@]3(O)[C@@](C)([C@H](C4=CC(=O)OC4)CC3)C[C@@H](O)[C@H]21 LPMXVESGRSUGHW-GHYGWZAOSA-N 0.000 claims description 38
244000166550 Strophanthus gratus Species 0.000 claims description 38
LPMXVESGRSUGHW-HBYQJFLCSA-N ouabain Chemical compound O[C@@H]1[C@H](O)[C@@H](O)[C@H](C)O[C@H]1O[C@@H]1C[C@@]2(O)CC[C@H]3[C@@]4(O)CC[C@H](C=5COC(=O)C=5)[C@@]4(C)C[C@@H](O)[C@@H]3[C@@]2(CO)[C@H](O)C1 LPMXVESGRSUGHW-HBYQJFLCSA-N 0.000 claims description 38
125000003275 alpha amino acid group Chemical group 0.000 claims description 31
239000002773 nucleotide Substances 0.000 claims description 31
125000003729 nucleotide group Chemical group 0.000 claims description 31
239000003446 ligand Substances 0.000 claims description 24
108090000623 proteins and genes Proteins 0.000 claims description 22
102000004169 proteins and genes Human genes 0.000 claims description 21
210000004027 cell Anatomy 0.000 claims description 14
108020004707 nucleic acids Proteins 0.000 claims description 14
102000039446 nucleic acids Human genes 0.000 claims description 14
150000007523 nucleic acids Chemical class 0.000 claims description 14
108020004414 DNA Proteins 0.000 claims description 10
241000894006 Bacteria Species 0.000 claims description 9
108020004705 Codon Proteins 0.000 claims description 4
241000206602 Eukaryota Species 0.000 claims description 2
241000238631 Hexapoda Species 0.000 claims description 2
240000004808 Saccharomyces cerevisiae Species 0.000 claims description 2
239000013612 plasmid Substances 0.000 claims description 2
230000002194 synthesizing effect Effects 0.000 claims description 2
230000001131 transforming effect Effects 0.000 claims description 2
108020004511 Recombinant DNA Proteins 0.000 claims 1
238000003780 insertion Methods 0.000 claims 1
230000037431 insertion Effects 0.000 claims 1
210000004962 mammalian cell Anatomy 0.000 claims 1
108020004999 messenger RNA Proteins 0.000 claims 1
102000002068 Glycopeptides Human genes 0.000 description 43
108010015899 Glycopeptides Proteins 0.000 description 43
230000000694 effects Effects 0.000 description 32
DQJCDTNMLBYVAY-ZXXIYAEKSA-N (2S,5R,10R,13R)-16-{[(2R,3S,4R,5R)-3-{[(2S,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy}-5-(ethylamino)-6-hydroxy-2-(hydroxymethyl)oxan-4-yl]oxy}-5-(4-aminobutyl)-10-carbamoyl-2,13-dimethyl-4,7,12,15-tetraoxo-3,6,11,14-tetraazaheptadecan-1-oic acid Chemical compound NCCCC[C@H](C(=O)N[C@@H](C)C(O)=O)NC(=O)CC[C@H](C(N)=O)NC(=O)[C@@H](C)NC(=O)C(C)O[C@@H]1[C@@H](NCC)C(O)O[C@H](CO)[C@H]1O[C@H]1[C@H](NC(C)=O)[C@@H](O)[C@H](O)[C@@H](CO)O1 DQJCDTNMLBYVAY-ZXXIYAEKSA-N 0.000 description 26
238000003556 assay Methods 0.000 description 25
108020003175 receptors Proteins 0.000 description 23
102000005962 receptors Human genes 0.000 description 23
239000011734 sodium Substances 0.000 description 22
102000003946 Prolactin Human genes 0.000 description 21
108010057464 Prolactin Proteins 0.000 description 21
238000006460 hydrolysis reaction Methods 0.000 description 21
229940097325 prolactin Drugs 0.000 description 21
150000001875 compounds Chemical class 0.000 description 18
230000007062 hydrolysis Effects 0.000 description 18
229940079593 drug Drugs 0.000 description 16
239000003814 drug Substances 0.000 description 16
229940088597 hormone Drugs 0.000 description 16
239000005556 hormone Substances 0.000 description 16
239000000203 mixture Substances 0.000 description 16
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 15
241000700159 Rattus Species 0.000 description 15
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 14
230000001817 pituitary effect Effects 0.000 description 14
239000000126 substance Substances 0.000 description 14
241000283973 Oryctolagus cuniculus Species 0.000 description 13
201000010099 disease Diseases 0.000 description 13
239000002243 precursor Substances 0.000 description 13
238000002474 experimental method Methods 0.000 description 12
210000002966 serum Anatomy 0.000 description 12
102000002710 Neurophysins Human genes 0.000 description 11
108010018674 Neurophysins Proteins 0.000 description 11
BQJCRHHNABKAKU-KBQPJGBKSA-N morphine Chemical compound O([C@H]1[C@H](C=C[C@H]23)O)C4=C5[C@@]12CCN(C)[C@@H]3CC5=CC=C4O BQJCRHHNABKAKU-KBQPJGBKSA-N 0.000 description 10
DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 9
230000005764 inhibitory process Effects 0.000 description 9
239000000047 product Substances 0.000 description 9
230000028327 secretion Effects 0.000 description 9
229910052708 sodium Inorganic materials 0.000 description 9
238000010186 staining Methods 0.000 description 9
230000001225 therapeutic effect Effects 0.000 description 9
238000002965 ELISA Methods 0.000 description 8
239000004480 active ingredient Substances 0.000 description 8
241001494479 Pecora Species 0.000 description 7
210000003016 hypothalamus Anatomy 0.000 description 7
239000000243 solution Substances 0.000 description 7
150000003431 steroids Chemical class 0.000 description 7
235000000346 sugar Nutrition 0.000 description 7
-1 troches Substances 0.000 description 7
108091006112 ATPases Proteins 0.000 description 6
102000057290 Adenosine Triphosphatases Human genes 0.000 description 6
241000208011 Digitalis Species 0.000 description 6
102000004190 Enzymes Human genes 0.000 description 6
108090000790 Enzymes Proteins 0.000 description 6
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
150000001413 amino acids Chemical class 0.000 description 6
239000008280 blood Substances 0.000 description 6
239000003795 chemical substances by application Substances 0.000 description 6
230000002401 inhibitory effect Effects 0.000 description 6
239000011780 sodium chloride Substances 0.000 description 6
206010062767 Hypophysitis Diseases 0.000 description 5
108060003951 Immunoglobulin Proteins 0.000 description 5
XNSAINXGIQZQOO-UHFFFAOYSA-N L-pyroglutamyl-L-histidyl-L-proline amide Natural products NC(=O)C1CCCN1C(=O)C(NC(=O)C1NC(=O)CC1)CC1=CN=CN1 XNSAINXGIQZQOO-UHFFFAOYSA-N 0.000 description 5
239000000627 Thyrotropin-Releasing Hormone Substances 0.000 description 5
102400000336 Thyrotropin-releasing hormone Human genes 0.000 description 5
101800004623 Thyrotropin-releasing hormone Proteins 0.000 description 5
OIPILFWXSMYKGL-UHFFFAOYSA-N acetylcholine Chemical compound CC(=O)OCC[N+](C)(C)C OIPILFWXSMYKGL-UHFFFAOYSA-N 0.000 description 5
229960004373 acetylcholine Drugs 0.000 description 5
239000006185 dispersion Substances 0.000 description 5
102000018358 immunoglobulin Human genes 0.000 description 5
210000003734 kidney Anatomy 0.000 description 5
239000000463 material Substances 0.000 description 5
229960005181 morphine Drugs 0.000 description 5
239000002858 neurotransmitter agent Substances 0.000 description 5
210000003635 pituitary gland Anatomy 0.000 description 5
XNSAINXGIQZQOO-SRVKXCTJSA-N protirelin Chemical compound NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H]1NC(=O)CC1)CC1=CN=CN1 XNSAINXGIQZQOO-SRVKXCTJSA-N 0.000 description 5
239000003488 releasing hormone Substances 0.000 description 5
229940034199 thyrotropin-releasing hormone Drugs 0.000 description 5
108091032973 (ribonucleotides)n+m Proteins 0.000 description 4
108010064733 Angiotensins Proteins 0.000 description 4
102000015427 Angiotensins Human genes 0.000 description 4
108020004394 Complementary RNA Proteins 0.000 description 4
BXSABLKMKAINIU-UHFFFAOYSA-N Oubagenin Natural products CC12CC(O)C(C3(C(O)CC(O)CC3(O)CC3)CO)C3C1(O)CCC2C1=CC(=O)OC1 BXSABLKMKAINIU-UHFFFAOYSA-N 0.000 description 4
102400000050 Oxytocin Human genes 0.000 description 4
101800000989 Oxytocin Proteins 0.000 description 4
XNOPRXBHLZRZKH-UHFFFAOYSA-N Oxytocin Natural products N1C(=O)C(N)CSSCC(C(=O)N2C(CCC2)C(=O)NC(CC(C)C)C(=O)NCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(CCC(N)=O)NC(=O)C(C(C)CC)NC(=O)C1CC1=CC=C(O)C=C1 XNOPRXBHLZRZKH-UHFFFAOYSA-N 0.000 description 4
239000007983 Tris buffer Substances 0.000 description 4
239000002671 adjuvant Substances 0.000 description 4
238000001042 affinity chromatography Methods 0.000 description 4
210000004369 blood Anatomy 0.000 description 4
239000002775 capsule Substances 0.000 description 4
238000004587 chromatography analysis Methods 0.000 description 4
239000003184 complementary RNA Substances 0.000 description 4
VYFYYTLLBUKUHU-UHFFFAOYSA-N dopamine Chemical compound NCCC1=CC=C(O)C(O)=C1 VYFYYTLLBUKUHU-UHFFFAOYSA-N 0.000 description 4
230000029142 excretion Effects 0.000 description 4
239000000284 extract Substances 0.000 description 4
239000004615 ingredient Substances 0.000 description 4
230000003993 interaction Effects 0.000 description 4
210000004731 jugular vein Anatomy 0.000 description 4
239000007788 liquid Substances 0.000 description 4
238000004519 manufacturing process Methods 0.000 description 4
210000004522 neurosecretory neuron Anatomy 0.000 description 4
BXSABLKMKAINIU-QOHCMMFCSA-N ouabagenin Chemical compound C1([C@H]2CC[C@]3(O)[C@H]4[C@@H]([C@]5([C@H](O)C[C@H](O)C[C@@]5(O)CC4)CO)[C@H](O)C[C@@]32C)=CC(=O)OC1 BXSABLKMKAINIU-QOHCMMFCSA-N 0.000 description 4
XNOPRXBHLZRZKH-DSZYJQQASA-N oxytocin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSC[C@H](N)C(=O)N1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)NCC(N)=O)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 XNOPRXBHLZRZKH-DSZYJQQASA-N 0.000 description 4
229960001723 oxytocin Drugs 0.000 description 4
230000012495 positive regulation of renal sodium excretion Effects 0.000 description 4
230000003389 potentiating effect Effects 0.000 description 4
239000003826 tablet Substances 0.000 description 4
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 4
210000002700 urine Anatomy 0.000 description 4
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
SFLSHLFXELFNJZ-QMMMGPOBSA-N (-)-norepinephrine Chemical compound NC[C@H](O)C1=CC=C(O)C(O)=C1 SFLSHLFXELFNJZ-QMMMGPOBSA-N 0.000 description 3
108010074725 Alpha,alpha-trehalose phosphorylase Proteins 0.000 description 3
102400000739 Corticotropin Human genes 0.000 description 3
101800000414 Corticotropin Proteins 0.000 description 3
241000233866 Fungi Species 0.000 description 3
206010020772 Hypertension Diseases 0.000 description 3
102000000588 Interleukin-2 Human genes 0.000 description 3
108010002350 Interleukin-2 Proteins 0.000 description 3
229930182555 Penicillin Natural products 0.000 description 3
DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
238000010521 absorption reaction Methods 0.000 description 3
239000011149 active material Substances 0.000 description 3
150000001412 amines Chemical class 0.000 description 3
125000000539 amino acid group Chemical group 0.000 description 3
210000003484 anatomy Anatomy 0.000 description 3
238000006243 chemical reaction Methods 0.000 description 3
238000000576 coating method Methods 0.000 description 3
IDLFZVILOHSSID-OVLDLUHVSA-N corticotropin Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)NC(=O)[C@@H](N)CO)C1=CC=C(O)C=C1 IDLFZVILOHSSID-OVLDLUHVSA-N 0.000 description 3
229960000258 corticotropin Drugs 0.000 description 3
AAOVKJBEBIDNHE-UHFFFAOYSA-N diazepam Chemical compound N=1CC(=O)N(C)C2=CC=C(Cl)C=C2C=1C1=CC=CC=C1 AAOVKJBEBIDNHE-UHFFFAOYSA-N 0.000 description 3
229960003529 diazepam Drugs 0.000 description 3
239000002612 dispersion medium Substances 0.000 description 3
239000003937 drug carrier Substances 0.000 description 3
210000003527 eukaryotic cell Anatomy 0.000 description 3
238000001802 infusion Methods 0.000 description 3
230000006651 lactation Effects 0.000 description 3
239000012528 membrane Substances 0.000 description 3
244000005700 microbiome Species 0.000 description 3
229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 3
BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 3
229960002748 norepinephrine Drugs 0.000 description 3
SFLSHLFXELFNJZ-UHFFFAOYSA-N norepinephrine Natural products NCC(O)C1=CC=C(O)C(O)=C1 SFLSHLFXELFNJZ-UHFFFAOYSA-N 0.000 description 3
239000003921 oil Substances 0.000 description 3
235000019198 oils Nutrition 0.000 description 3
239000008194 pharmaceutical composition Substances 0.000 description 3
239000004033 plastic Substances 0.000 description 3
229920003023 plastic Polymers 0.000 description 3
238000011533 pre-incubation Methods 0.000 description 3
210000001236 prokaryotic cell Anatomy 0.000 description 3
238000003127 radioimmunoassay Methods 0.000 description 3
230000002829 reductive effect Effects 0.000 description 3
239000002904 solvent Substances 0.000 description 3
208000024891 symptom Diseases 0.000 description 3
238000012360 testing method Methods 0.000 description 3
239000005495 thyroid hormone Substances 0.000 description 3
229940036555 thyroid hormone Drugs 0.000 description 3
DTQVDTLACAAQTR-UHFFFAOYSA-N trifluoroacetic acid Substances OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 3
YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
239000000275 Adrenocorticotropic Hormone Substances 0.000 description 2
101800001288 Atrial natriuretic factor Proteins 0.000 description 2
102400001282 Atrial natriuretic peptide Human genes 0.000 description 2
101800001890 Atrial natriuretic peptide Proteins 0.000 description 2
206010010904 Convulsion Diseases 0.000 description 2
229920002261 Corn starch Polymers 0.000 description 2
XUIIKFGFIJCVMT-GFCCVEGCSA-N D-thyroxine Chemical compound IC1=CC(C[C@@H](N)C(O)=O)=CC(I)=C1OC1=CC(I)=C(O)C(I)=C1 XUIIKFGFIJCVMT-GFCCVEGCSA-N 0.000 description 2
206010017600 Galactorrhoea Diseases 0.000 description 2
108010010803 Gelatin Proteins 0.000 description 2
206010018910 Haemolysis Diseases 0.000 description 2
URLZCHNOLZSCCA-VABKMULXSA-N Leu-enkephalin Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=CC=C1 URLZCHNOLZSCCA-VABKMULXSA-N 0.000 description 2
229910019142 PO4 Inorganic materials 0.000 description 2
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
241000282887 Suidae Species 0.000 description 2
102000011923 Thyrotropin Human genes 0.000 description 2
108010061174 Thyrotropin Proteins 0.000 description 2
108010003205 Vasoactive Intestinal Peptide Proteins 0.000 description 2
102400000015 Vasoactive intestinal peptide Human genes 0.000 description 2
241000700605 Viruses Species 0.000 description 2
230000009471 action Effects 0.000 description 2
230000001919 adrenal effect Effects 0.000 description 2
230000001270 agonistic effect Effects 0.000 description 2
238000004458 analytical method Methods 0.000 description 2
230000003042 antagnostic effect Effects 0.000 description 2
239000005557 antagonist Substances 0.000 description 2
239000003242 anti bacterial agent Substances 0.000 description 2
230000000844 anti-bacterial effect Effects 0.000 description 2
230000003302 anti-idiotype Effects 0.000 description 2
229940121375 antifungal agent Drugs 0.000 description 2
239000003429 antifungal agent Substances 0.000 description 2
238000004166 bioassay Methods 0.000 description 2
230000000035 biogenic effect Effects 0.000 description 2
230000015572 biosynthetic process Effects 0.000 description 2
229960002685 biotin Drugs 0.000 description 2
239000011616 biotin Substances 0.000 description 2
230000037396 body weight Effects 0.000 description 2
239000000872 buffer Substances 0.000 description 2
150000001720 carbohydrates Chemical group 0.000 description 2
235000014633 carbohydrates Nutrition 0.000 description 2
230000003177 cardiotonic effect Effects 0.000 description 2
NSQLIUXCMFBZME-MPVJKSABSA-N carperitide Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 NSQLIUXCMFBZME-MPVJKSABSA-N 0.000 description 2
OSASVXMJTNOKOY-UHFFFAOYSA-N chlorobutanol Chemical compound CC(C)(O)C(Cl)(Cl)Cl OSASVXMJTNOKOY-UHFFFAOYSA-N 0.000 description 2
239000004020 conductor Substances 0.000 description 2
238000010276 construction Methods 0.000 description 2
239000008120 corn starch Substances 0.000 description 2
230000001419 dependent effect Effects 0.000 description 2
238000010586 diagram Methods 0.000 description 2
238000000502 dialysis Methods 0.000 description 2
229960003638 dopamine Drugs 0.000 description 2
239000012530 fluid Substances 0.000 description 2
235000003599 food sweetener Nutrition 0.000 description 2
238000009472 formulation Methods 0.000 description 2
108010074605 gamma-Globulins Proteins 0.000 description 2
229920000159 gelatin Polymers 0.000 description 2
239000008273 gelatin Substances 0.000 description 2
235000019322 gelatine Nutrition 0.000 description 2
235000011852 gelatine desserts Nutrition 0.000 description 2
108060003552 hemocyanin Proteins 0.000 description 2
230000008588 hemolysis Effects 0.000 description 2
230000003054 hormonal effect Effects 0.000 description 2
JYGXADMDTFJGBT-VWUMJDOOSA-N hydrocortisone Chemical compound O=C1CC[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 JYGXADMDTFJGBT-VWUMJDOOSA-N 0.000 description 2
230000002267 hypothalamic effect Effects 0.000 description 2
210000000987 immune system Anatomy 0.000 description 2
238000012760 immunocytochemical staining Methods 0.000 description 2
208000015181 infectious disease Diseases 0.000 description 2
239000003112 inhibitor Substances 0.000 description 2
238000002347 injection Methods 0.000 description 2
239000007924 injection Substances 0.000 description 2
230000002452 interceptive effect Effects 0.000 description 2
238000001990 intravenous administration Methods 0.000 description 2
VBUWHHLIZKOSMS-RIWXPGAOSA-N invicorp Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)C(C)C)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=C(O)C=C1 VBUWHHLIZKOSMS-RIWXPGAOSA-N 0.000 description 2
239000007951 isotonicity adjuster Substances 0.000 description 2
230000007774 longterm Effects 0.000 description 2
HQKMJHAJHXVSDF-UHFFFAOYSA-L magnesium stearate Chemical compound [Mg+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O HQKMJHAJHXVSDF-UHFFFAOYSA-L 0.000 description 2
238000005259 measurement Methods 0.000 description 2
230000001404 mediated effect Effects 0.000 description 2
230000003278 mimic effect Effects 0.000 description 2
210000002569 neuron Anatomy 0.000 description 2
210000002963 paraventricular hypothalamic nucleus Anatomy 0.000 description 2
150000002960 penicillins Chemical class 0.000 description 2
239000000813 peptide hormone Substances 0.000 description 2
230000000144 pharmacologic effect Effects 0.000 description 2
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
239000010452 phosphate Substances 0.000 description 2
239000006187 pill Substances 0.000 description 2
229920001223 polyethylene glycol Polymers 0.000 description 2
210000004896 polypeptide structure Anatomy 0.000 description 2
239000000843 powder Substances 0.000 description 2
239000003755 preservative agent Substances 0.000 description 2
230000002265 prevention Effects 0.000 description 2
238000000746 purification Methods 0.000 description 2
230000002441 reversible effect Effects 0.000 description 2
238000003860 storage Methods 0.000 description 2
238000007920 subcutaneous administration Methods 0.000 description 2
239000000758 substrate Substances 0.000 description 2
239000003765 sweetening agent Substances 0.000 description 2
238000003786 synthesis reaction Methods 0.000 description 2
239000006188 syrup Substances 0.000 description 2
235000020357 syrup Nutrition 0.000 description 2
229960000874 thyrotropin Drugs 0.000 description 2
230000001748 thyrotropin Effects 0.000 description 2
229940034208 thyroxine Drugs 0.000 description 2
XUIIKFGFIJCVMT-UHFFFAOYSA-N thyroxine-binding globulin Natural products IC1=CC(CC([NH3+])C([O-])=O)=CC(I)=C1OC1=CC(I)=C(O)C(I)=C1 XUIIKFGFIJCVMT-UHFFFAOYSA-N 0.000 description 2
238000005303 weighing Methods 0.000 description 2
ZGEGCLOFRBLKSE-UHFFFAOYSA-N 1-Heptene Chemical class CCCCCC=C ZGEGCLOFRBLKSE-UHFFFAOYSA-N 0.000 description 1
IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
VOXZDWNPVJITMN-ZBRFXRBCSA-N 17β-estradiol Chemical compound OC1=CC=C2[C@H]3CC[C@](C)([C@H](CC4)O)[C@@H]4[C@@H]3CCC2=C1 VOXZDWNPVJITMN-ZBRFXRBCSA-N 0.000 description 1
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
244000215068 Acacia senegal Species 0.000 description 1
241000014654 Adna Species 0.000 description 1
102000002260 Alkaline Phosphatase Human genes 0.000 description 1
108020004774 Alkaline Phosphatase Proteins 0.000 description 1
GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
241000272525 Anas platyrhynchos Species 0.000 description 1
241000416162 Astragalus gummifer Species 0.000 description 1
IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 1
108090001008 Avidin Proteins 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
241000282465 Canis Species 0.000 description 1
241001631457 Cannula Species 0.000 description 1
239000000055 Corticotropin-Releasing Hormone Substances 0.000 description 1
108010022152 Corticotropin-Releasing Hormone Proteins 0.000 description 1
102000012289 Corticotropin-Releasing Hormone Human genes 0.000 description 1
206010011224 Cough Diseases 0.000 description 1
GUBGYTABKSRVRQ-WFVLMXAXSA-N DEAE-cellulose Chemical compound OC1C(O)C(O)C(CO)O[C@H]1O[C@@H]1C(CO)OC(O)C(O)C1O GUBGYTABKSRVRQ-WFVLMXAXSA-N 0.000 description 1
102000053602 DNA Human genes 0.000 description 1
101710088194 Dehydrogenase Proteins 0.000 description 1
QXNVGIXVLWOKEQ-UHFFFAOYSA-N Disodium Chemical compound [Na][Na] QXNVGIXVLWOKEQ-UHFFFAOYSA-N 0.000 description 1
102400000242 Dynorphin A(1-17) Human genes 0.000 description 1
108010065372 Dynorphins Proteins 0.000 description 1
241000272060 Elapidae Species 0.000 description 1
241000196324 Embryophyta Species 0.000 description 1
240000009088 Fragaria x ananassa Species 0.000 description 1
108700012941 GNRH1 Proteins 0.000 description 1
239000000579 Gonadotropin-Releasing Hormone Substances 0.000 description 1
102000018997 Growth Hormone Human genes 0.000 description 1
108010051696 Growth Hormone Proteins 0.000 description 1
239000000095 Growth Hormone-Releasing Hormone Substances 0.000 description 1
102000038461 Growth Hormone-Releasing Hormone Human genes 0.000 description 1
229920000084 Gum arabic Polymers 0.000 description 1
101001123843 Homo sapiens Nucleolus and neural progenitor protein Proteins 0.000 description 1
GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
102000009151 Luteinizing Hormone Human genes 0.000 description 1
108010073521 Luteinizing Hormone Proteins 0.000 description 1
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
239000004472 Lysine Substances 0.000 description 1
241000124008 Mammalia Species 0.000 description 1
229920001410 Microfiber Polymers 0.000 description 1
108050004114 Monellin Proteins 0.000 description 1
208000012902 Nervous system disease Diseases 0.000 description 1
208000025966 Neurological disease Diseases 0.000 description 1
101710138657 Neurotoxin Proteins 0.000 description 1
102100028752 Nucleolus and neural progenitor protein Human genes 0.000 description 1
108091034117 Oligonucleotide Proteins 0.000 description 1
108010093625 Opioid Peptides Proteins 0.000 description 1
102000001490 Opioid Peptides Human genes 0.000 description 1
241000237988 Patellidae Species 0.000 description 1
JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
102000003992 Peroxidases Human genes 0.000 description 1
240000004713 Pisum sativum Species 0.000 description 1
235000010582 Pisum sativum Nutrition 0.000 description 1
102000006877 Pituitary Hormones Human genes 0.000 description 1
108010047386 Pituitary Hormones Proteins 0.000 description 1
239000002202 Polyethylene glycol Substances 0.000 description 1
229920002873 Polyethylenimine Polymers 0.000 description 1
ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
RJKFOVLPORLFTN-LEKSSAKUSA-N Progesterone Chemical class C1CC2=CC(=O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H](C(=O)C)[C@@]1(C)CC2 RJKFOVLPORLFTN-LEKSSAKUSA-N 0.000 description 1
102000013009 Pyruvate Kinase Human genes 0.000 description 1
108020005115 Pyruvate Kinase Proteins 0.000 description 1
241000711798 Rabies lyssavirus Species 0.000 description 1
241000702263 Reovirus sp. Species 0.000 description 1
241000555745 Sciuridae Species 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
229920002684 Sepharose Polymers 0.000 description 1
229920001800 Shellac Polymers 0.000 description 1
101710142969 Somatoliberin Proteins 0.000 description 1
AUYYCJSJGJYCDS-LBPRGKRZSA-N Thyrolar Chemical compound IC1=CC(C[C@H](N)C(O)=O)=CC(I)=C1OC1=CC=C(O)C(I)=C1 AUYYCJSJGJYCDS-LBPRGKRZSA-N 0.000 description 1
229920001615 Tragacanth Polymers 0.000 description 1
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
210000001015 abdomen Anatomy 0.000 description 1
238000002835 absorbance Methods 0.000 description 1
239000003070 absorption delaying agent Substances 0.000 description 1
239000000205 acacia gum Substances 0.000 description 1
235000010489 acacia gum Nutrition 0.000 description 1
239000000370 acceptor Substances 0.000 description 1
239000013543 active substance Substances 0.000 description 1
239000003329 adenohypophysis hormone Substances 0.000 description 1
239000000556 agonist Substances 0.000 description 1
239000000783 alginic acid Substances 0.000 description 1
235000010443 alginic acid Nutrition 0.000 description 1
229920000615 alginic acid Polymers 0.000 description 1
229960001126 alginic acid Drugs 0.000 description 1
150000004781 alginic acids Chemical class 0.000 description 1
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
229910052921 ammonium sulfate Inorganic materials 0.000 description 1
238000012870 ammonium sulfate precipitation Methods 0.000 description 1
235000011130 ammonium sulphate Nutrition 0.000 description 1
210000004198 anterior pituitary gland Anatomy 0.000 description 1
239000007864 aqueous solution Substances 0.000 description 1
230000001746 atrial effect Effects 0.000 description 1
239000012752 auxiliary agent Substances 0.000 description 1
210000003050 axon Anatomy 0.000 description 1
230000008901 benefit Effects 0.000 description 1
239000011230 binding agent Substances 0.000 description 1
230000004071 biological effect Effects 0.000 description 1
235000020958 biotin Nutrition 0.000 description 1
210000004556 brain Anatomy 0.000 description 1
239000006189 buccal tablet Substances 0.000 description 1
210000004899 c-terminal region Anatomy 0.000 description 1
150000003943 catecholamines Chemical class 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
230000008859 change Effects 0.000 description 1
238000001311 chemical methods and process Methods 0.000 description 1
238000007385 chemical modification Methods 0.000 description 1
239000003153 chemical reaction reagent Substances 0.000 description 1
150000001805 chlorine compounds Chemical class 0.000 description 1
229960004926 chlorobutanol Drugs 0.000 description 1
238000012875 competitive assay Methods 0.000 description 1
230000036461 convulsion Effects 0.000 description 1
230000008878 coupling Effects 0.000 description 1
238000010168 coupling process Methods 0.000 description 1
238000005859 coupling reaction Methods 0.000 description 1
230000009260 cross reactivity Effects 0.000 description 1
238000001514 detection method Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
230000018109 developmental process Effects 0.000 description 1
235000005911 diet Nutrition 0.000 description 1
230000037213 diet Effects 0.000 description 1
UGMCXQCYOVCMTB-UHFFFAOYSA-K dihydroxy(stearato)aluminium Chemical compound CCCCCCCCCCCCCCCCCC(=O)O[Al](O)O UGMCXQCYOVCMTB-UHFFFAOYSA-K 0.000 description 1
238000010790 dilution Methods 0.000 description 1
239000012895 dilution Substances 0.000 description 1
229910001873 dinitrogen Inorganic materials 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
239000007884 disintegrant Substances 0.000 description 1
208000035475 disorder Diseases 0.000 description 1
238000006073 displacement reaction Methods 0.000 description 1
239000002934 diuretic Substances 0.000 description 1
239000002552 dosage form Substances 0.000 description 1
231100000673 dose–response relationship Toxicity 0.000 description 1
239000003480 eluent Substances 0.000 description 1
239000002158 endotoxin Chemical group 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
238000001952 enzyme assay Methods 0.000 description 1
210000003743 erythrocyte Anatomy 0.000 description 1
229960005309 estradiol Drugs 0.000 description 1
229930182833 estradiol Natural products 0.000 description 1
BEFDCLMNVWHSGT-UHFFFAOYSA-N ethenylcyclopentane Chemical compound C=CC1CCCC1 BEFDCLMNVWHSGT-UHFFFAOYSA-N 0.000 description 1
230000001747 exhibiting effect Effects 0.000 description 1
210000003722 extracellular fluid Anatomy 0.000 description 1
238000001914 filtration Methods 0.000 description 1
238000005048 flame photometry Methods 0.000 description 1
235000013305 food Nutrition 0.000 description 1
239000012634 fragment Substances 0.000 description 1
238000004108 freeze drying Methods 0.000 description 1
230000005714 functional activity Effects 0.000 description 1
108010047064 gamma-Endorphin Proteins 0.000 description 1
239000007789 gas Substances 0.000 description 1
239000007903 gelatin capsule Substances 0.000 description 1
239000011521 glass Substances 0.000 description 1
239000000122 growth hormone Substances 0.000 description 1
108091005708 gustatory receptors Proteins 0.000 description 1
230000036541 health Effects 0.000 description 1
230000002949 hemolytic effect Effects 0.000 description 1
238000004128 high performance liquid chromatography Methods 0.000 description 1
230000003284 homeostatic effect Effects 0.000 description 1
108091008039 hormone receptors Proteins 0.000 description 1
229960000890 hydrocortisone Drugs 0.000 description 1
239000000960 hypophysis hormone Substances 0.000 description 1
230000003053 immunization Effects 0.000 description 1
238000002649 immunization Methods 0.000 description 1
238000003018 immunoassay Methods 0.000 description 1
238000003365 immunocytochemistry Methods 0.000 description 1
230000002163 immunogen Effects 0.000 description 1
229940072221 immunoglobulins Drugs 0.000 description 1
238000011532 immunohistochemical staining Methods 0.000 description 1
230000001771 impaired effect Effects 0.000 description 1
238000002513 implantation Methods 0.000 description 1
238000000099 in vitro assay Methods 0.000 description 1
238000001727 in vivo Methods 0.000 description 1
230000000415 inactivating effect Effects 0.000 description 1
230000002779 inactivation Effects 0.000 description 1
238000010348 incorporation Methods 0.000 description 1
239000003701 inert diluent Substances 0.000 description 1
239000007972 injectable composition Substances 0.000 description 1
230000000968 intestinal effect Effects 0.000 description 1
238000007918 intramuscular administration Methods 0.000 description 1
238000007912 intraperitoneal administration Methods 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
239000008101 lactose Substances 0.000 description 1
150000002605 large molecules Chemical class 0.000 description 1
235000010445 lecithin Nutrition 0.000 description 1
239000000787 lecithin Substances 0.000 description 1
229940067606 lecithin Drugs 0.000 description 1
230000000670 limiting effect Effects 0.000 description 1
XMGQYMWWDOXHJM-UHFFFAOYSA-N limonene Chemical compound CC(=C)C1CCC(C)=CC1 XMGQYMWWDOXHJM-UHFFFAOYSA-N 0.000 description 1
150000002632 lipids Chemical group 0.000 description 1
229920006008 lipopolysaccharide Chemical group 0.000 description 1
239000000314 lubricant Substances 0.000 description 1
229940040129 luteinizing hormone Drugs 0.000 description 1
229920002521 macromolecule Polymers 0.000 description 1
235000019359 magnesium stearate Nutrition 0.000 description 1
239000002609 medium Substances 0.000 description 1
230000002503 metabolic effect Effects 0.000 description 1
125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
235000010270 methyl p-hydroxybenzoate Nutrition 0.000 description 1
239000003658 microfiber Substances 0.000 description 1
235000013336 milk Nutrition 0.000 description 1
239000008267 milk Substances 0.000 description 1
210000004080 milk Anatomy 0.000 description 1
208000008013 morphine dependence Diseases 0.000 description 1
230000001452 natriuretic effect Effects 0.000 description 1
230000000926 neurological effect Effects 0.000 description 1
239000002581 neurotoxin Substances 0.000 description 1
231100000618 neurotoxin Toxicity 0.000 description 1
239000002547 new drug Substances 0.000 description 1
150000002825 nitriles Chemical class 0.000 description 1
229910052757 nitrogen Inorganic materials 0.000 description 1
231100000252 nontoxic Toxicity 0.000 description 1
230000003000 nontoxic effect Effects 0.000 description 1
PTVIBIVJSXWMPT-FGSANIJTSA-N octadecaneuropeptide Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@@H](N)CCC(N)=O)[C@@H](C)O)C(C)C)C(C)C)[C@@H](C)O PTVIBIVJSXWMPT-FGSANIJTSA-N 0.000 description 1
239000003399 opiate peptide Substances 0.000 description 1
230000003287 optical effect Effects 0.000 description 1
239000007968 orange flavor Substances 0.000 description 1
210000000056 organ Anatomy 0.000 description 1
239000002245 particle Substances 0.000 description 1
229940049954 penicillin Drugs 0.000 description 1
108040007629 peroxidase activity proteins Proteins 0.000 description 1
239000000546 pharmaceutical excipient Substances 0.000 description 1
229960003742 phenol Drugs 0.000 description 1
239000002953 phosphate buffered saline Substances 0.000 description 1
238000005375 photometry Methods 0.000 description 1
229920005862 polyol Polymers 0.000 description 1
150000003077 polyols Chemical class 0.000 description 1
229920001282 polysaccharide Chemical group 0.000 description 1
239000005017 polysaccharide Chemical group 0.000 description 1
150000004804 polysaccharides Chemical group 0.000 description 1
239000011148 porous material Substances 0.000 description 1
210000001883 posterior pituitary gland Anatomy 0.000 description 1
239000011591 potassium Substances 0.000 description 1
229910052700 potassium Inorganic materials 0.000 description 1
229920001592 potato starch Polymers 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
238000002360 preparation method Methods 0.000 description 1
239000000583 progesterone congener Substances 0.000 description 1
230000002035 prolonged effect Effects 0.000 description 1
230000001737 promoting effect Effects 0.000 description 1
235000010232 propyl p-hydroxybenzoate Nutrition 0.000 description 1
230000009257 reactivity Effects 0.000 description 1
230000008707 rearrangement Effects 0.000 description 1
230000008929 regeneration Effects 0.000 description 1
238000011069 regeneration method Methods 0.000 description 1
238000009877 rendering Methods 0.000 description 1
238000011160 research Methods 0.000 description 1
230000000241 respiratory effect Effects 0.000 description 1
230000004044 response Effects 0.000 description 1
108010004790 ribonuclease S-peptide Proteins 0.000 description 1
CVHZOJJKTDOEJC-UHFFFAOYSA-N saccharin Chemical compound C1=CC=C2C(=O)NS(=O)(=O)C2=C1 CVHZOJJKTDOEJC-UHFFFAOYSA-N 0.000 description 1
229940081974 saccharin Drugs 0.000 description 1
235000019204 saccharin Nutrition 0.000 description 1
239000000901 saccharin and its Na,K and Ca salt Substances 0.000 description 1
150000003839 salts Chemical class 0.000 description 1
239000000565 sealant Substances 0.000 description 1
230000003248 secreting effect Effects 0.000 description 1
239000004208 shellac Substances 0.000 description 1
ZLGIYFNHBLSMPS-ATJNOEHPSA-N shellac Chemical compound OCCCCCC(O)C(O)CCCCCCCC(O)=O.C1C23[C@H](C(O)=O)CCC2[C@](C)(CO)[C@@H]1C(C(O)=O)=C[C@@H]3O ZLGIYFNHBLSMPS-ATJNOEHPSA-N 0.000 description 1
229940113147 shellac Drugs 0.000 description 1
235000013874 shellac Nutrition 0.000 description 1
239000007787 solid Substances 0.000 description 1
235000010199 sorbic acid Nutrition 0.000 description 1
229940075582 sorbic acid Drugs 0.000 description 1
239000004334 sorbic acid Substances 0.000 description 1
238000010561 standard procedure Methods 0.000 description 1
230000001954 sterilising effect Effects 0.000 description 1
238000004659 sterilization and disinfection Methods 0.000 description 1
239000003270 steroid hormone Substances 0.000 description 1
235000021012 strawberries Nutrition 0.000 description 1
150000008163 sugars Chemical class 0.000 description 1
230000001629 suppression Effects 0.000 description 1
239000004094 surface-active agent Substances 0.000 description 1
238000001356 surgical procedure Methods 0.000 description 1
239000000725 suspension Substances 0.000 description 1
238000013268 sustained release Methods 0.000 description 1
239000012730 sustained-release form Substances 0.000 description 1
125000000383 tetramethylene group Chemical group [H]C([H])([*:1])C([H])([H])C([H])([H])C([H])([H])[*:2] 0.000 description 1
239000000892 thaumatin Substances 0.000 description 1
235000010436 thaumatin Nutrition 0.000 description 1
210000001519 tissue Anatomy 0.000 description 1
230000032258 transport Effects 0.000 description 1
229940035722 triiodothyronine Drugs 0.000 description 1
239000001226 triphosphate Substances 0.000 description 1
235000011178 triphosphate Nutrition 0.000 description 1
UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 1
238000001291 vacuum drying Methods 0.000 description 1
238000003828 vacuum filtration Methods 0.000 description 1
LSGOVYNHVSXFFJ-UHFFFAOYSA-N vanadate(3-) Chemical compound [O-][V]([O-])([O-])=O LSGOVYNHVSXFFJ-UHFFFAOYSA-N 0.000 description 1
230000002227 vasoactive effect Effects 0.000 description 1
235000015112 vegetable and seed oil Nutrition 0.000 description 1
239000008158 vegetable oil Substances 0.000 description 1
239000003981 vehicle Substances 0.000 description 1
210000003462 vein Anatomy 0.000 description 1
239000011782 vitamin Substances 0.000 description 1
229940088594 vitamin Drugs 0.000 description 1
229930003231 vitamin Natural products 0.000 description 1
235000013343 vitamin Nutrition 0.000 description 1
235000012431 wafers Nutrition 0.000 description 1
GASYAMBJHBRTOE-WHDBNHDESA-N γ-endorphin Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=CC=C1 GASYAMBJHBRTOE-WHDBNHDESA-N 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/16—Oxytocins; Vasopressins; Related peptides
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids

Landscapes

Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Health & Medical Sciences (AREA)
Organic Chemistry (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Engineering & Computer Science (AREA)
Medicinal Chemistry (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Biophysics (AREA)
Genetics & Genomics (AREA)
Biomedical Technology (AREA)
Urology & Nephrology (AREA)
Immunology (AREA)
Hematology (AREA)
Cell Biology (AREA)
Microbiology (AREA)
Biotechnology (AREA)
Food Science & Technology (AREA)
Physics & Mathematics (AREA)
Analytical Chemistry (AREA)
General Physics & Mathematics (AREA)
Pathology (AREA)
Peptides Or Proteins (AREA)
Investigating Or Analysing Biological Materials (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)

JP1050208A 1988-03-04 1989-03-03 非ペプチドのペプチド相当物及びそのデザイン方法 Pending JPH02104595A (ja)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US16392688A	1988-03-04	1988-03-04
US163926		1988-03-04

Publications (1)

Publication Number	Publication Date
JPH02104595A true JPH02104595A (ja)	1990-04-17

Family

ID=22592208

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP1050208A Pending JPH02104595A (ja)	1988-03-04	1989-03-03	非ペプチドのペプチド相当物及びそのデザイン方法

Country Status (5)

Country	Link
EP (1)	EP0331184A3 (de)
JP (1)	JPH02104595A (de)
AU (1)	AU3101989A (de)
DK (1)	DK105289A (de)
IL (1)	IL89487A0 (de)

Families Citing this family (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPH09508355A (ja) *	1993-12-09	1997-08-26	チバ−ガイギーアクチェンゲゼルシャフト	組合せ化合物ライブラリーの製法
WO1996012186A1 (en) *	1994-10-14	1996-04-25	Chiron Mimotopes Pty. Ltd.	Method and apparatus for efficient mimotope discovery
GB0025251D0 (en) *	2000-10-14	2000-11-29	Proteom Ltd	Antisense peptides to Fc receptors and their uses

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5077195A (en) *	1985-03-01	1991-12-31	Board Of Reagents, The University Of Texas System	Polypeptides complementary to peptides or proteins having an amino acid sequence or nucleotide coding sequence at least partially known and methods of design therefor

1989
- 1989-03-03 DK DK105289A patent/DK105289A/da not_active Application Discontinuation
- 1989-03-03 JP JP1050208A patent/JPH02104595A/ja active Pending
- 1989-03-03 EP EP19890103755 patent/EP0331184A3/de not_active Withdrawn
- 1989-03-05 IL IL89487A patent/IL89487A0/xx unknown
- 1989-03-06 AU AU31019/89A patent/AU3101989A/en not_active Abandoned

Also Published As

Publication number	Publication date
EP0331184A2 (de)	1989-09-06
DK105289A (da)	1989-09-05
DK105289D0 (da)	1989-03-03
IL89487A0 (en)	1989-09-10
AU3101989A (en)	1989-09-07
EP0331184A3 (de)	1991-05-08

Publication	Publication Date	Title
Karlsson	1979	Chemistry of protein toxins in snake venoms
Mason et al.	1984	Release of the predicted calcitonin gene-related peptide from cultured rat trigeminal ganglion cells
Spannagel et al.	1996	Purification and characterization of a luminal cholecystokinin-releasing factor from rat intestinal secretion.
JP2879079B2 (ja)	1999-04-05	成長ホルモンレセプター
FI90255B (fi)	1993-09-30	Menetelmä polypeptidin valmistamiseksi, joka on komplementaarinen ainakin osalle alkuperäistä peptidiä tai proteiinia, ja komplementaarisen polypeptidin käyttö
US4833166A (en)	1989-05-23	Growth hormone releasing hormone complementary peptides
JPH0669390B2 (ja)	1994-09-07	ヒト−レニンに対するモノクロ−ナル抗体及びその使用
EP2662389B1 (de)	2019-03-13	Verfahren zur herstellung eines antigens zur gewinnung eines antikörpers gegen hydrophobe peptide
EP0709455B1 (de)	1998-09-09	Monoklonaler Antikörper gegen menschliches Glicentin, Hybridoma zur Herstellung dieses Antikörpers und Testverfahren für menschliches Glicentin unter Verwendung dieses Antikörpers
Eysselein et al.	1983	Biological activity of canine intestinal cholecystokinin-58
DK175191B1 (da)	2004-07-05	Monoklonalt og polyklonalt antistof mod HbA1C
KR20090041416A (ko)	2009-04-28	비만증을 억제하는 백신 및 방법
US7264808B2 (en)	2007-09-04	Synthetic peptide for neurological disorders
PT92885B (pt)	1995-12-29	Processo de preparacao de moleculas cataliticas compreendendo um sitio de ligacao com anticorpos e contendo ioes metalicos polivalentes e de composicoes contendo as mesmas bem como processo de realizacao de uma reaccao quimica predeterminada
Li et al.	2020	Optimized functional and structural design of dual-target LMRAP, a bifunctional fusion protein with a 25-amino-acid antitumor peptide and GnRH Fc fragment
DK168710B1 (da)	1994-05-24	Monoklont antistof eller fragment deraf, immunogen, immunanalysefremgangsmåde til bestemmelse af glycosyleret nativt humant albumin, peptid samt immunanalysesæt
JP2003503019A (ja)	2003-01-28	プレプチン機能を有するペプチド
EP0331184A2 (de)	1989-09-06	Peptid-Gegenwerte von Nichtpeptiden und Verfahren zum Entwurf dafür
JPH06505496A (ja)	1994-06-23	活性因子ｘ１１１の活性化を阻害するための組成物と方法
DK161095B (da)	1991-05-27	Fremgangsmaade til enzym-immunanalyse af pankreatisk glucagon og peptid-enzym-konjugat til brug ved denne fremgangsmaade
Beall et al.	1973	Neutralizing and non-neutralizing antibodies to bovine thyroid-stimulating hormone and its subunits
JPH03504248A (ja)	1991-09-19	外来抗原に対する寛容の誘発
CN118047851B (zh)	2025-05-16	一种针对原肌球蛋白受体激酶d5结构域的高亲和力d-蛋白抑制剂及其用途
Lehrman et al.	1992	Identification and characterization of an anti-isoaspartic acid monoclonal antibody
JPH0570484A (ja)	1993-03-23	ペプチドおよびその塩